ArticlePlant physiology2009
The two plastidial starch-related dikinases sequentially phosphorylate glucosyl residues at the surface of both the A- and B-type allomorphs of crystallized maltodextrins but the mode of action differs.
Article in Plant physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed, 77 citations in OpenAlex.
- Solving the Insoluble: Regulation of α-Polyglucan Solubility and Functionality in Nature.Molecules (Basel, Switzerland) · 2026Review
- Regulatory factors of starch metabolism in cereal endosperm.Plant molecular biology · 2026Review
- Covalently linked phosphate monoesters on alpha-polyglucans reduce substrate affinity of branching enzymes.Carbohydrate polymers · 2025Article
- Genome-wide identification of the AcBAM family in kiwifruit (Actinidia chinensis cv. Hongyang) and the expression profiling analysis of AcBAMs reveal their role in starch metabolism.BMC plant biology · 2025Article
- Target of rapamycin signaling regulates starch degradation via α-glucan water dikinase in a unicellular red alga.Plant physiology · 2025Article
- Branched oligosaccharides cause atypical starch granule initiation in Arabidopsis chloroplasts.Plant physiology · 2025Article
- Article
- Starch phosphorylation-A needle in a haystack.Plant methods · 2024Article
- Starch phosphorylation regulates starch granule morphological homogeneity in Arabidopsis thaliana.Plant physiology · 2024Article
- Assessing the impacts of genetic defects on starch metabolism inJournal of the Royal Society, Interface · 2023Article
- Investigation into the structure of crystalline maltodextrin particles by second harmonic generation microscopy.Biomedical optics express · 2023Article
- Efficient Accumulation of Amylopectin and Its Molecular Mechanism in the Submerged Duckweed Mutant.International journal of molecular sciences · 2023Article
- Starch degradation in the bean fruit pericarp is characterized by an increase in maltose metabolism.Physiologia plantarum · 2022Article
- BETA-AMYLASE9 is a plastidial nonenzymatic regulator of leaf starch degradation.Plant physiology · 2022Article
- EARLY STARVATION 1 Is a Functionally Conserved Protein Promoting Gravitropic Responses in Plants by Forming Starch Granules.Frontiers in plant science · 2021Article
- LIKE SEX4 1 Acts as a β-Amylase-Binding Scaffold on Starch Granules during Starch Degradation.The Plant cell · 2019Article
- Modification of Cassava Root Starch Phosphorylation Enhances Starch Functional Properties.Frontiers in plant science · 2018Article
- Abnormal glycogen chain length pattern, not hyperphosphorylation, is critical in Lafora disease.EMBO molecular medicine · 2017Article
- Transitory Starch Metabolism in Guard Cells: Unique Features for a Unique Function.Plant physiology · 2017Review
- Starch phosphorylation: insights and perspectives.Cellular and molecular life sciences : CMLS · 2016Review
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4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this study, two crystallized maltodextrins were generated that consist of the same oligoglucan pattern but differ strikingly in the physical order of double helices. As revealed by x-ray diffraction, they represent the highly ordered A- and B-type allomorphs. Both crystallized maltodextrins were similar in size distribution and birefringence. They were used as model substrates to study the consecutive action of the two starch-related dikinases, the glucan, water dikinase and the phosphoglucan, water dikinase. The glucan, water dikinase and the phosphoglucan, water dikinase selectively esterify glucosyl residues in the C6 and C3 positions, respectively. Recombinant glucan, water dikinase phosphorylated both allomorphs with similar rates and caused complete glucan solubilization. Soluble neutral maltodextrins inhibited the glucan, water dikinase-mediated phosphorylation of crystalline particles. Recombinant phosphoglucan, water dikinase phosphorylated both the A- and B-type allomorphs only following a prephosphorylation by the glucan, water dikinase, and the activity increased with the extent of prephosphorylation. The action of the phosphoglucan, water dikinase on the prephosphorylated A- and B-type allomorphs differed. When acting on the B-type allomorph, by far more phosphoglucans were solubilized as compared with the A type. However, with both allomorphs, the phosphoglucan, water dikinase formed significant amounts of monophosphorylated phosphoglucans. Thus, the enzyme is capable of acting on neutral maltodextrins. It is concluded that the actual carbohydrate substrate of the phosphoglucan, water dikinase is defined by physical rather than by chemical parameters. A model is proposed that explains, at the molecular level, the consecutive action of the two starch-related dikinases.
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